| 1995 |
Tastin (TROAP) is a cytoplasmic protein necessary for trophinin to function as a cell adhesion molecule; trophinin and tastin associate with the cytoskeleton and mediate divalent cation-independent homophilic cell adhesion between trophoblastic and endometrial epithelial cells at their apical surfaces. |
Expression cDNA cloning, cell adhesion assays between HT-H and SNG-M cell lines |
Genes & development |
Medium |
7758945
|
| 1998 |
Tastin (TROAP) does not directly bind trophinin; instead, a third cytoplasmic protein, bystin, directly binds both trophinin and tastin, and this binding is enhanced by the presence of cytokeratin 8 and 18 as a third molecule. Tastin co-localizes with trophinin, bystin, and cytokeratins in HT-H cells. |
Yeast two-hybrid assays, in vitro protein binding assays (GST pulldown), immunocytochemistry |
Proceedings of the National Academy of Sciences of the United States of America |
High |
9560222
|
| 2002 |
Tastin (TROAP) is a microtubule-associated protein; its N-terminal basic region mediates direct microtubule binding. Tastin co-sediments with polymerized microtubules and disperses to the cytoplasm upon nocodazole-induced microtubule depolymerization. Tastin also directly binds Tctex-1, a light chain of cytoplasmic dynein, as confirmed by yeast two-hybrid, co-immunoprecipitation, and in vitro GST-pulldown. |
Microtubule sedimentation assay, nocodazole treatment, N- and C-terminal deletion mutant analysis, yeast two-hybrid, co-immunoprecipitation, GST-Tctex-1 pulldown with in vitro translated tastin |
The Biochemical journal |
High |
12049630
|
| 2008 |
Tastin (TROAP) is required for bipolar spindle assembly and centrosome integrity during mitosis. Tastin protein levels peak in G2/M phase. Tastin localizes to microtubules, centrosomes, and the mitotic spindle. Tastin interacts with dynein intermediate chain, p150(Glued) (dynactin component), and gamma-tubulin in addition to Tctex-1. Overexpression causes monopolar spindle formation; depletion causes multipolar spindles through fragmentation of pericentrosomal material and centriole splitting, exclusively during mitosis and dependent on microtubule integrity and Eg5 activity. Tastin depletion does not disrupt NuMA or p150(Glued) localization at spindle poles. |
siRNA knockdown, overexpression, immunofluorescence microscopy, co-immunoprecipitation, flow cytometry (cell cycle), nocodazole and Eg5-inhibitor treatment |
FASEB journal |
High |
18218922
|
| 2021 |
TROAP directly binds DYRK1A/B, causing cytoplasmic retention of DYRK1A/B and promoting cell cycle progression via activation of Akt/GSK-3β signaling in hepatocellular carcinoma cells. |
Co-immunoprecipitation, shRNA knockdown, overexpression, in vitro and in vivo tumor growth assays, western blot for Akt/GSK-3β pathway |
Cell death & disease |
Medium |
33500384
|
| 2021 |
In prostate cancer cells, TROAP functions downstream of EZH2 and activates the TWIST/c-Myc pathway to promote cell proliferation, migration, and invasion; overexpression of TWIST partially rescues the inhibitory effects of TROAP knockdown. |
Lentiviral shRNA knockdown, overexpression rescue assay, Transwell assay, flow cytometry, western blot, bioinformatic correlation analysis |
Frontiers in oncology |
Medium |
33692939
|
| 2021 |
TROAP activates the Wnt/β-Catenin signaling pathway in glioma cells and promotes cell proliferation, migration, and invasion; silencing β-Catenin or Axin2 reverses the tumor-promoting effects of TROAP overexpression, placing TROAP upstream of Wnt/β-Catenin. |
shRNA knockdown, overexpression vector, epistasis rescue (β-Catenin/Axin2 silencing), CCK-8, colony formation, Transwell, flow cytometry, immunofluorescence, western blot, GSEA |
CNS neuroscience & therapeutics |
Medium |
34077623
|
| 2022 |
METTL14-mediated m6A RNA methylation promotes TROAP mRNA degradation/instability; loss of METTL14 in ovarian cancer stabilizes TROAP mRNA and increases TROAP protein, promoting cancer cell proliferation. |
MeRIP-qPCR, RNA stability assay (actinomycin D), METTL14 overexpression, TROAP siRNA, luciferase reporter assay, cDNA microarray, immunohistochemistry |
Frontiers in oncology |
Medium |
35251990
|
| 2023 |
TROAP physically interacts with STAT3 in kidney renal clear cell carcinoma cells to promote tumor proliferation, migration, and metastasis; this interaction was identified by co-immunoprecipitation followed by shotgun LC-MS and validated by functional rescue experiments. |
Co-immunoprecipitation, shotgun LC-MS/MS, qRT-PCR, western blot, Celigo, MTT, wound healing, flow cytometry, xenograft model, functional rescue assay |
International journal of molecular sciences |
Medium |
37298609
|
| 2024 |
The transcription factor E2F1 directly activates TROAP transcription; E2F1 overexpression increases TROAP expression and promotes endometrial cancer cell proliferation, migration, and glycolysis in a TROAP-dependent manner. |
Dual luciferase reporter assay, qRT-PCR, western blot, siRNA knockdown, rescue experiments with TROAP knockdown, xenograft mouse model |
Histology and histopathology |
Medium |
39501799
|
| 2024 |
PCBP2 (an RNA-binding protein) directly binds TROAP mRNA and stabilizes it in gastric cancer cells; PCBP2 depletion reduces TROAP mRNA half-life and suppresses GC cell proliferation, migration, invasion, and promotes ferroptosis. |
RIP (RNA immunoprecipitation) assay, actinomycin D RNA stability assay, siRNA knockdown, western blot, functional assays (EdU, wound healing, Transwell), xenograft model |
Naunyn-Schmiedeberg's archives of pharmacology |
Medium |
39586843
|
| 2025 |
FBXW5 promotes ubiquitination-mediated degradation of KLF13; loss of KLF13 increases TROAP transcription (KLF13 suppresses TROAP promoter activity), thereby facilitating EMT in lung adenocarcinoma. TROAP overexpression reverses KLF13-mediated inhibition of invasion, migration, and EMT. |
Co-immunoprecipitation (FBXW5–KLF13 interaction), ChIP assay, dual luciferase reporter gene assay (KLF13 binding to TROAP promoter), overexpression rescue, western blot, Transwell, wound healing, CCK-8, xenograft |
Molecular carcinogenesis |
Medium |
40696794
|
| 2025 |
TROAP promotes chemoresistance in colorectal cancer cells via de novo lipogenesis driven by histone acetylation and PI3K/Akt pathway activation, as evidenced by increased lipid droplet formation and altered PI3K/Akt signaling upon TROAP manipulation. |
Nile red staining (lipid droplet), western blot, flow cytometry, CCK-8, Transwell, proteomic and bioinformatics analysis, xenograft model |
Functional & integrative genomics |
Low |
41350492
|